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Open data
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Basic information
Entry | Database: PDB / ID: 2k6t | ||||||
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Title | Solution structure of the relaxin-like factor | ||||||
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![]() | HORMONE / protein / Cleavage on pair of basic residues / Disease mutation / Polymorphism / Secreted | ||||||
Function / homology | ![]() Relaxin receptors / positive regulation of cAMP-mediated signaling / oocyte maturation / positive regulation of wound healing / positive regulation of epithelial cell migration / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / G protein-coupled receptor binding / insulin receptor binding / hormone activity / male gonad development ...Relaxin receptors / positive regulation of cAMP-mediated signaling / oocyte maturation / positive regulation of wound healing / positive regulation of epithelial cell migration / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / G protein-coupled receptor binding / insulin receptor binding / hormone activity / male gonad development / cell-cell signaling / G alpha (s) signalling events / spermatogenesis / protease binding / negative regulation of cell population proliferation / signaling receptor binding / positive regulation of cell population proliferation / negative regulation of apoptotic process / perinuclear region of cytoplasm / extracellular space / extracellular region Similarity search - Function | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing | ||||||
![]() | Bullesbach, E.E. / Hass, M.A.S. / Jensen, M.R. / Hansen, D.F. / Kristensen, S.M. / Schwabe, C. / Led, J.J. | ||||||
![]() | ![]() Title: Solution structure of a conformationally restricted fully active derivative of the human relaxin-like factor Authors: Bullesbach, E.E. / Hass, M.A.S. / Jensen, M.R. / Hansen, D.F. / Kristensen, S.M. / Schwabe, C. / Led, J.J. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 335 KB | Display | ![]() |
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PDB format | ![]() | 289.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 354.3 KB | Display | ![]() |
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Full document | ![]() | 607 KB | Display | |
Data in XML | ![]() | 26.4 KB | Display | |
Data in CIF | ![]() | 41.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 2778.189 Da / Num. of mol.: 1 / Fragment: UNP residues 106-131 / Source method: obtained synthetically / Details: This sequence occurs naturally in humans. / References: UniProt: P51460 |
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#2: Protein/peptide | Mass: 3528.118 Da / Num. of mol.: 1 / Fragment: UNP residues 25-55 / Source method: obtained synthetically / Details: This sequence occurs naturally in humans. / References: UniProt: P51460 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: structure was determined using homonuclear NOE |
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Sample preparation
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Sample conditions |
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-NMR measurement
NMR spectrometer |
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Processing
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Refinement | Method: torsion angle dynamics, simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 1154 / NOE intraresidue total count: 506 / NOE long range total count: 182 / NOE medium range total count: 208 / NOE sequential total count: 258 | ||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 / Maximum lower distance constraint violation: 0 Å / Maximum upper distance constraint violation: 6 Å / Representative conformer: 1 | ||||||||||||||||||||||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0.053 Å / Distance rms dev error: 0.0015 Å |